A Kinetic Study of Acetylcholinesterase Inhibition by Fractions of Oleo diox Roxb.leaf and Curculigo orchioides Gaertn Rhizome for the Treatment of Alzheimer’s Disease
European Journal of Medicinal Plants,
Introduction and Aim: Acetylcholinesterase (AChE) has an important role in the biochemical studies indicating that AChE accelerates the formation of amyloid-β fibril and forms AChE-Aβ complexes in the brain. The medicinal plants of Curculigoorchioides Gaertn., and Oleo diox Roxb. collected from Western Ghat region of Kodagu, Karnataka, India have many medicinal values such as antioxidant, anti-cancer, anti-diabetic, neuroprotective activity and anti-inflammatory property. Aim of the study was to check whether C. orchioides Gaertn. and Oleo diox Roxb. fractions significantly inhibit acetylcholinesterase in different concentration-dependent manner(1-3 mg/mL).
Results: Plant fraction concentrations resulted in >60%AChE inhibition as compared with the standard Galantamine. The IC50 value was 0.15 mg/mL which was calculated from the equation of the percentage inhibition curve for the test or plant fraction. The Lineweaver-Burk plot indicated that the fraction followed competitive and non-competitive inhibition kinetics. Finally, we conclude that the type of plot exhibited by the C. orchioides Gaertn. and Oleo dioxRoxb. fractions has a possible therapeutic application for improving memory and other cognitive functions.The medicinal plant-based drugs are known to have limitations due to their fewer side effects and problems associated with bioavailability, which necessitates the interest in finding better AChE inhibitors from plant sources.
- amyloid-β fibril
- C. Orchioides Gaertn
- Oleo diox Roxb fraction
- Lineweaver-Burk plot.
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Lineweaver H, Burk D. The determination of enzyme dissociation constants. Journal of the American Chemical Society. 1934;56(3):658-666.
Ahmed M, Latif N, Khan R, Ahmad A, Rocha JBT, Mazzanti CM, et al. Enzymatic and biochemical characterization of Bungarussindanus snake venom acety-lcholinesterase. Journal of Venomous Animals and Toxins including Tropical Diseases. 2012;18(2):236-243.
Sassa A, Beard WA, Shock DD, Wilson SH. Steady-state, pre-steady-state and single-turnover kinetic measurement for DNA glycosylase activity. Journal of Visualized Experiments. 2013;(78):50-95.
Ashraf M, Ahmad K, Ahmad I, Ahmad S, Arshad S, Shah SMS, et al. Acety-lcholinesterase and NADH oxidase inhibitory activity of some medicinal plants. J. Med. Plants Res. 2011;5(10):2086-2089.
Bagewadi Z, Baligar P. Phytoconstituents investigation by lc-ms and evaluation of anti- microbial and anti-pyretic properties of cynodondactylon. IJPSR. 2014;5(7): 2874-2889.
Tung BT, Thu DK, Thu NTK, Hai NT. Antioxidant and acetylcholinesterase inhibitory activities of ginger root (Zingiber Officinale Roscoe) extract. Journal of Complementary and Integrative Medicine. 2017;14(4):1-15.
Kumar S, Seal CJ, Okello EJ. Kinetics of acetylcholinesterase inhibition by an aqueous extract of Withania somnifera roots. International Journal of Pharma-ceutical Sciences and Research.2018;2:1- 7.
James D, Harvey L, David B. Molecular cell biology, scientific American Books, W. H. Freeman and Co., New York, NY, Gamete Research. 2015;17(1):95-195.
Baldwin RL. Structure and mechanism in protein science. A guide to enzyme catalysis and protein folding. Protein Science. 2008;9(1):207-211.
Pratap GK, Ashwani S, Manjula S. Alzheimer’s disease: A challenge in managing with certain medicinal plants- Areview. IJPSR. 2017;8(12):4960-4972.
De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes Amyloid β-Peptide fibril formation†. Bio-chemistry. 2001;40(35):10447-10457.
Howes MJR, Houghton PJ. Plants used in Chinese and Indian traditional medicine for improvement of memory and cognitive function. Pharmacology Biochemistry and Behavior. 2003;75(3):513-527.
Kamal MA, Greig NH, Alhomida AS, Al-Jafari AA. Kinetics of human acetylcholinesterase inhibition by the novel experimental alzheimer therapeutic agent, tolserine. Biochemical Pharmacology. 2000;60(4):561-570.
Knapp MJ. A 30-week randomized controlled trial of high-dose tacrine in patients with Alzheimer’s disease. The Tacrine Study Group. JAMA: The Journal of the American Medical Association. 1994;271(13):985-991.
Lahiri DK, Farlow MR, Greig NH, Sambamurti K. Current drug targets for Alzheimer’s disease treatment. Drug Development Research. 2002;56(3):267-281.
Michaelis L, Menten M. The original Michaelis constant: translation of the 1913 Michaelis-Menten paper. Biochemistry. 2011;450(39):8264-9.
Pohanka M, Hrabinova M. Kuca K, Simonato JP. Assessment of Acety-lcholinesterase Activity Using Indoxy-lacetate and Comparison with the Standard Ellman’s Method. International Journal of Molecular Sciences. 2011; 12(4):2631-2640.
Saleem M, Jamous R, Yousef S. In-vitro screening of acetylcholinesterase inhibitory activity of extracts from Palestinian indigenous flora in relation to the treatment of Alzheimer’s disease. Functional Foods in Health and Disease. 2014;4(9):381- 400.
Soni N, Singh DK, Singh VK. Inhibition kinetics of acetylcholinesterase and phosphatases by the active constituents of Terminalia arjuna and Tamarindus indica in the Cerebral Ganglion of Lymnaea acuminata. Pharmacognosy Journal. 2017; 9(2):148-156.
Wetwitay aklung P, Limmatvapirat C, Phaechamud T, Keokitichai S. Kinetics of acetylcholinesterase inhibition of Quisqualis indica Linn. Flower extract. kinetics of acetylcholinesterase inhibition silpakorn U science and Tech J. 2007; 1(2):20-28.
Pohanka M, Hrabinova M, Kuca K, Simonato JP. Assessment of acety-lcholinesterase activity using indoxy-lacetate and comparison with the Standard Ellman’s Method. International Journal of Molecular Sciences. 2011;12(4):2631-2640.
Sobhani R, Pal AK, Bhattacharjee A, Mitra S, Aguan K. Screening indigenous medicinal plants of Northeast India for Their anti-alzheimer’s properties. Pharma-cognosy Journal. 2016;9(1):46-54.
Croghan PC. Modeling dynamic phenomena in molecular and cellular biology. By L. E. Segel. Quarterly Journal of Experimental Physiology. 1985;70(4): 642-656.
Chowdhury S, Kumar S. In vitro anti-acetylcholinesterase activity of an aqueous extract of Unicariatomentosa and in silico study of its active constituents. Bio-information. 2016;12(3):112-118.
Niño J, Hernández JA, Correa YM, Mosquera OM. In vitro inhibition of acet-ylcholinesterase by crude plant extracts from Colombian flora. Memórias do Instituto Oswaldo Cruz. 2006;101(7):783-785.
Kumar S, Chowdhury S. Kinetics of acetylcholinesterase inhibition by an aqueous extract of Cuminum cyminum seeds. International Journal of Applied Sciences and Biotechnology. 2014;2(1): 64-68.
Wszelaki N, Kuciun A, Kiss A. Screening of traditional European herbal medicines for acetylcholinesterase and butyrylcholinesterase inhibitory activity. Acta Pharmaceutica. 2010;60(1).
Zechel DL, Konermann L, Withers SG, Douglas DJ. Pre-steady state kinetic analysis of an enzymatic reaction monitored by time-resolved electrospray Ionization mass spectrometry. Bio-chemistry. 1998;37(21):7664-7669.
Deveci E, Tel-Çayan G, Duru ME. Essential oil composition, antioxidant, anticholinesterase and anti-tyrosinase activities of two Turkish plant species: Ferula eleocharis and Sideritis stricta. Natural Product Communications. 2018; 13(1):13-18.
Murata K, Tanaka K, Akiyama R, Noro I, Nishio A, Nakagawa S, et al. Anti-cholinesterase activity of crude drugs selected from the ingredients of incense sticks and heartwood of Chamaecyparis obtusa. Natural Product Communications. 2018;13(7):15-26.
Sichaem J, Tip-pyang S, Lugsanangarm K. Bioactive aporphine alkaloids from the Roots of Artabotrys Spinosus: Cholinesterase inhibitory activity and molecular docking studies. Natural Product Communications. 2018;13(10):1-
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